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    Crystallization and preliminary X-ray diffraction data for a purple acid phosphatase from sweet potato


    Schenk, Gerhard and Carrington, Lyle E. and Hamilton, Susan E. and de Jersey, John and Guddat, Luke W. (1999) Crystallization and preliminary X-ray diffraction data for a purple acid phosphatase from sweet potato. Acta Crystallographica Section D Biological Crystallography, 55 (12). pp. 2051-2052. ISSN 0907-4449

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    Abstract

    Purple acid phosphatase from sweet potato is a homodimer of 110 kDa. Two forms of the enzyme have been characterized. One contains an Fe±Zn centre similar to that previously reported for red kidney bean purple acid phosphatase. Another isoform, the subject of this work, is the ®rst con®rmed example of an Fe±Mn-containing enzyme. Crystals of this protein have been grown from PEG 6000. They have unit-cell parameters a = b = 118.4, c = 287.4 A Ê and have the symmetry of space group P6522, with one dimer per asymmetric unit. Diffraction data collected using a conventional X-ray source from a cryocooled crystal extend to 2.90 A Ê resolution. The three-dimensional structure of the enzyme will provide insight into the coordination of this novel binuclear metal centre.

    Item Type: Article
    Keywords: binuclear metal centre; metalloenzyme; purple acid phosphatase; protein crystallization;
    Academic Unit: Faculty of Science and Engineering > Chemistry
    Item ID: 3686
    Depositing User: Gary Schenk
    Date Deposited: 28 May 2012 13:07
    Journal or Publication Title: Acta Crystallographica Section D Biological Crystallography
    Publisher: International Union of Crystallography
    Refereed: Yes
    URI:

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